Tauler A, Carreras J
Comp Biochem Physiol B. 1987;87(1):117-24. doi: 10.1016/0305-0491(87)90478-0.
2,3-Bisphosphoglycerate synthase-phosphatase and the hybrid phosphoglycerate mutase/2,3-bisphosphoglycerate synthase-phosphatase have been partially purified from pig brain. Their 2,3-bisphosphoglycerate synthase, 2,3-bisphosphoglycerate phosphatase and phosphoglycerate mutase activities are concurrently lost upon heating and treatment with reagents specific for histidyl, arginyl and lysyl residues. The two enzymes differ in their thermal stability and sensitivity to tetrathionate. Substrates and cofactors protect against inactivation, the protective effects varying with the modifying reagent. The synthase activity of both enzymes shows a nonhyperbolic pattern which fits to a second degree polynomial. The Km, Ki and optimum pH values are similar to those of the 2,3-bisphosphoglycerate synthase-phosphatase from erythrocytes and the hybrid enzyme from skeletal muscle. The synthase activity is inhibited by inorganic phosphate and it is stimulated by glycolyate 2-P.
已从猪脑中部分纯化出2,3-二磷酸甘油酸合酶-磷酸酶以及杂合磷酸甘油酸变位酶/2,3-二磷酸甘油酸合酶-磷酸酶。经加热以及用对组氨酸、精氨酸和赖氨酸残基具有特异性的试剂处理后，它们的2,3-二磷酸甘油酸合酶、2,3-二磷酸甘油酸磷酸酶和磷酸甘油酸变位酶活性会同时丧失。这两种酶在热稳定性和对连四硫酸盐的敏感性方面存在差异。底物和辅因子可防止酶失活，保护作用因修饰试剂而异。两种酶的合酶活性均呈现非双曲线模式，符合二次多项式。其米氏常数（Km）、抑制常数（Ki）和最适pH值与红细胞中的2,3-二磷酸甘油酸合酶-磷酸酶以及骨骼肌中的杂合酶相似。合酶活性受到无机磷酸盐的抑制，并被2-磷酸乙醇酸激活。
